ID A0A0M8Z1Z4_9ACTN Unreviewed; 610 AA.
AC A0A0M8Z1Z4;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=5'-nucleotidase {ECO:0000313|EMBL:KOX47216.1};
GN ORFNames=ADL09_14830 {ECO:0000313|EMBL:KOX47216.1};
OS Streptomyces sp. NRRL F-7442.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1519498 {ECO:0000313|EMBL:KOX47216.1, ECO:0000313|Proteomes:UP000037772};
RN [1] {ECO:0000313|EMBL:KOX47216.1, ECO:0000313|Proteomes:UP000037772}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL F-7442 {ECO:0000313|EMBL:KOX47216.1,
RC ECO:0000313|Proteomes:UP000037772};
RA Noorani M.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the 5'-nucleotidase family.
CC {ECO:0000256|RuleBase:RU362119}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KOX47216.1}.
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DR EMBL; LGEH01000142; KOX47216.1; -; Genomic_DNA.
DR RefSeq; WP_053663788.1; NZ_LGEH01000142.1.
DR AlphaFoldDB; A0A0M8Z1Z4; -.
DR PATRIC; fig|1519498.3.peg.3074; -.
DR OrthoDB; 1016457at2; -.
DR Proteomes; UP000037772; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0009166; P:nucleotide catabolic process; IEA:InterPro.
DR CDD; cd07412; MPP_YhcR_N; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR Gene3D; 3.90.780.10; 5'-Nucleotidase, C-terminal domain; 1.
DR InterPro; IPR008334; 5'-Nucleotdase_C.
DR InterPro; IPR036907; 5'-Nucleotdase_C_sf.
DR InterPro; IPR006179; 5_nucleotidase/apyrase.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR041831; YhcR_MPP.
DR PANTHER; PTHR11575:SF48; 5' NUCLEOTIDASE, ECTO-LIKE; 1.
DR PANTHER; PTHR11575; 5'-NUCLEOTIDASE-RELATED; 1.
DR Pfam; PF02872; 5_nucleotid_C; 1.
DR Pfam; PF00149; Metallophos; 1.
DR PRINTS; PR01607; APYRASEFAMLY.
DR SUPFAM; SSF55816; 5'-nucleotidase (syn. UDP-sugar hydrolase), C-terminal domain; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU362119};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362119};
KW Signal {ECO:0000256|RuleBase:RU362119}.
FT SIGNAL 1..33
FT /evidence="ECO:0000256|RuleBase:RU362119"
FT CHAIN 34..610
FT /evidence="ECO:0000256|RuleBase:RU362119"
FT /id="PRO_5039750188"
FT DOMAIN 70..325
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF00149"
FT DOMAIN 406..569
FT /note="5'-Nucleotidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02872"
FT REGION 39..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 72..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 610 AA; 64031 MW; 5D22125BF55862E5 CRC64;
MPATAPSHQP RRRRRTSRLL VAAATVVTAG ALAAAALPAS ASTGGNGRGN DGQGQGHGQG
RYQDIQLLSF NDLHGNLEPP AGSSGRVTEV QPDGTTETVD AGGVEYLATH LREARKGNRY
SITAAGGDMV GASPLLSGLF HDEPTIEALN QLDLDVTSVG NHEFDEGARE LARLQNGGCH
PTEGCYTDKT FKGADFPYLA ANVLDEKTKK PILKPYWVWK QNGVKVGFIG VTLEGTPGIV
SAEGVKGLTF KDEVETINKY AKELQRQGVK SIVALIHEGG FPASSSYNYD CDSPGAGDGV
SGPIVDIARN ITPQVDALVT GHTHNAYVCT IPDPAGNPRT VTSASSFGRL YTDTTLTYDR
ATGDIARTSV KSANHVVTRD VPKAPDMTRL IDRWNTLAAP IGNRPVGYVT ADINRDGTES
PLGDLIADAQ FAYGKEQDPE TDLALMNPGG IRAPLTYAAS GAEGDGVVTY AEAFTVQPFA
NTVNLKDYTG AQLIQVLKEQ VSGPNEAAPK ILQVSSGLTY TLDLTKSGAD RVVTDSIRLN
GAPVDENATY RVASNSFLAG GGDGFTTLGE GTNESVGADD LAAFEQYLTA NSSAGSPLAP
PAADRITVVR
//